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Matching Observed Alpha Helix Lengths to Predicted Secondary Structure



Brian D. Cloteaux, Nadezhda Serova


Because of the complexity in determining the 3D structure of a protein, the use of partial information determined from experimental techniques can greatly reduce the overall computational expense. We investigate the problem of matching experimentally observed lengths of helices to the predicted secondary structure of a protein. We give a simple and fast algorithm for producing a library of possible solutions. Then we test our algorithm by performing a series of computational experiments of predicting the alpha helix placement of proteins with an already known order. These tests seem to demonstrate that our method, if given a good prediction of the protein s secondary structure, can generate high quality lists of potential placements of the helix length onto the protein sequences.
Proceedings Title
Computational Structural Bioinformatics Workshop
Conference Dates
November 1-4, 2009
Conference Location
Washington, DC


protein structure, randomized algorithm


Cloteaux, B. and Serova, N. (2009), Matching Observed Alpha Helix Lengths to Predicted Secondary Structure, Computational Structural Bioinformatics Workshop, Washington, DC, [online], (Accessed June 23, 2024)


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Created November 1, 2009, Updated February 19, 2017